KAPS_SACPS
ID KAPS_SACPS Reviewed; 202 AA.
AC Q9C2Y6;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE Short=APS kinase;
GN Name=MET14;
OS Saccharomyces pastorianus (Lager yeast) (Saccharomyces cerevisiae x
OS Saccharomyces eubayanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=27292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M204;
RX PubMed=12702335; DOI=10.1111/j.1567-1364.2002.tb00050.x;
RA Johannesen P.F., Hansen J.;
RT "Differential transcriptional regulation of sulfur assimilation gene
RT homologues in the Saccharomyces carlsbergensis yeast species hybrid.";
RL FEMS Yeast Res. 1:315-322(2002).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; AY017216; AAK00577.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C2Y6; -.
DR SMR; Q9C2Y6; -.
DR UniPathway; UPA00140; UER00205.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Kinase;
KW Methionine biosynthesis; Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN 1..202
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105935"
FT ACT_SITE 105
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 23059 MW; 12433EB6BBA67AFD CRC64;
MATNITWHPN LTYDERKELR KQDGCTVWLT GLSASGKSTI ACALEQLLLQ KNLSAYRLDG
DNIRFGLNKD LGFSEKDRNE NIRRISEVSK LFADSCAVSI TSFISPYRVD RDRARDLHKE
AGLKFIEIFV DVPLEVAEQR DPKGLYKKAR EGVIKEFTGI SAPYEAPKAP ELHLRTDQKT
VEECAAIIYE YLVNEKIIRK HL